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A divalent antibody format is required for neutralization of human cytomegalovirus via antigenic domain 2 on glycoprotein B

Lantto, Johan LU ; Fletcher, Jean M and Ohlin, Mats LU (2002) In Journal of General Virology 83(Pt 8). p.2001-2005
Abstract
Glycoprotein B (gB) of human cytomegalovirus (HCMV) is the dominating protein in the envelope of this virus and gives rise to virus-neutralizing antibodies in most infected individuals. We have previously isolated a neutralizing human antibody specific for antigenic domain 2 (AD-2) on gB, a poorly immunogenic epitope, which nevertheless is capable of eliciting potent neutralizing antibodies. In order to define parameters important for the neutralization of HCMV via gB, we have investigated the virus-neutralizing capacity and the kinetics of the interaction with AD-2 of the monomeric and dimeric forms of a single chain variable fragment (scFv) corresponding to this antibody. We demonstrate here that neutralization of HCMV via AD-2 on gB can... (More)
Glycoprotein B (gB) of human cytomegalovirus (HCMV) is the dominating protein in the envelope of this virus and gives rise to virus-neutralizing antibodies in most infected individuals. We have previously isolated a neutralizing human antibody specific for antigenic domain 2 (AD-2) on gB, a poorly immunogenic epitope, which nevertheless is capable of eliciting potent neutralizing antibodies. In order to define parameters important for the neutralization of HCMV via gB, we have investigated the virus-neutralizing capacity and the kinetics of the interaction with AD-2 of the monomeric and dimeric forms of a single chain variable fragment (scFv) corresponding to this antibody. We demonstrate here that neutralization of HCMV via AD-2 on gB can be mediated by dimeric scFv, while monomeric fragments cannot mediate neutralization of the virus, despite a slow dissociation from the intact glycoprotein. This finding is discussed in the context of possible mechanisms for antibody-mediated virus neutralization. (Less)
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author
organization
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type
Contribution to journal
publication status
published
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in
Journal of General Virology
volume
83
issue
Pt 8
pages
2001 - 2005
publisher
Society for General Microbiology
external identifiers
  • pmid:12124464
  • wos:000176989900019
  • scopus:0036322438
ISSN
1465-2099
language
English
LU publication?
yes
id
dd6176c6-8f80-467a-89c6-467693d42e6e (old id 109429)
alternative location
http://www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12124464&dopt=Abstract
date added to LUP
2007-07-09 09:48:19
date last changed
2017-08-27 05:08:51
@article{dd6176c6-8f80-467a-89c6-467693d42e6e,
  abstract     = {Glycoprotein B (gB) of human cytomegalovirus (HCMV) is the dominating protein in the envelope of this virus and gives rise to virus-neutralizing antibodies in most infected individuals. We have previously isolated a neutralizing human antibody specific for antigenic domain 2 (AD-2) on gB, a poorly immunogenic epitope, which nevertheless is capable of eliciting potent neutralizing antibodies. In order to define parameters important for the neutralization of HCMV via gB, we have investigated the virus-neutralizing capacity and the kinetics of the interaction with AD-2 of the monomeric and dimeric forms of a single chain variable fragment (scFv) corresponding to this antibody. We demonstrate here that neutralization of HCMV via AD-2 on gB can be mediated by dimeric scFv, while monomeric fragments cannot mediate neutralization of the virus, despite a slow dissociation from the intact glycoprotein. This finding is discussed in the context of possible mechanisms for antibody-mediated virus neutralization.},
  author       = {Lantto, Johan and Fletcher, Jean M and Ohlin, Mats},
  issn         = {1465-2099},
  language     = {eng},
  number       = {Pt 8},
  pages        = {2001--2005},
  publisher    = {Society for General Microbiology},
  series       = {Journal of General Virology},
  title        = {A divalent antibody format is required for neutralization of human cytomegalovirus via antigenic domain 2 on glycoprotein B},
  volume       = {83},
  year         = {2002},
}